ID A0A0P9DVL8_9ARCH Unreviewed; 380 AA.
AC A0A0P9DVL8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase {ECO:0000256|HAMAP-Rule:MF_01675};
DE EC=2.5.1.73 {ECO:0000256|HAMAP-Rule:MF_01675};
DE AltName: Full=Sep-tRNA:Cys-tRNA synthase {ECO:0000256|HAMAP-Rule:MF_01675};
DE Short=SepCysS {ECO:0000256|HAMAP-Rule:MF_01675};
GN ORFNames=AOA65_1061 {ECO:0000313|EMBL:KPV64175.1};
OS Candidatus Bathyarchaeota archaeon BA1.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV64175.1, ECO:0000313|Proteomes:UP000050312};
RN [1] {ECO:0000313|EMBL:KPV64175.1, ECO:0000313|Proteomes:UP000050312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA1 {ECO:0000313|EMBL:KPV64175.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
CC -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000256|HAMAP-Rule:MF_01675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-
CC cysteinyl-tRNA(Cys) + phosphate; Xref=Rhea:RHEA:25686, Rhea:RHEA-
CC COMP:9679, Rhea:RHEA-COMP:9719, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:78517, ChEBI:CHEBI:78551; EC=2.5.1.73;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01675};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01675};
CC -!- SUBUNIT: Homodimer. Interacts with SepRS. {ECO:0000256|HAMAP-
CC Rule:MF_01675}.
CC -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000256|HAMAP-
CC Rule:MF_01675}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01675}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV64175.1}.
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DR EMBL; LIHJ01000041; KPV64175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9DVL8; -.
DR STRING; 1700835.AOA65_1061; -.
DR KEGG; barc:AOA65_1061; -.
DR PATRIC; fig|1700835.3.peg.1756; -.
DR Proteomes; UP000050312; Unassembled WGS sequence.
DR GO; GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01675; Sep_Cys_tRNA_synth; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR013375; Sep_Cys-tRNA_synth_arc.
DR InterPro; IPR008829; SepSecS/SepCysS.
DR NCBIfam; TIGR02539; SepCysS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF3; O-PHOSPHO-L-SERYL-TRNA:CYS-TRNA SYNTHASE; 1.
DR Pfam; PF05889; SepSecS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01675};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01675};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01675}.
FT BINDING 190
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT BINDING 213..215
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
SQ SEQUENCE 380 AA; 42958 MW; 89B173C11A0A6B93 CRC64;
MSKGILSEWR AREELFINLE PLQRGGVVPA EARKVALSYV NGYSTCDHCL GTLHILKKPP
ICDFLIQVAE FLGMDRAIIT HGCREAKFAV MHAITKPGQA IVMDENKHYT SYVAAERAGL
KIYEVPSTGH PKFRVEPEEY ISAVEKVRKE TGELPMLVLL THVDGTYGNL VDAEKVGKIC
QEYNVPFLLN TAYSSGRMPI NGKKLLADFV TCSGHKSWAA GAGVVGILAI RDEWKDKVFK
PSQRYKVKPI EILGCSARGS STLVLMASFP YVMERVKHWD VEVEKARWFS NQMESLGDIR
QLGDKPHNHD LIRFETPVFD RIAQKHKRRG YFLYEELMKR KIVGIKAGKT KSFDLSTYGL
NKEQLSYVID SFKDIINKLS
//
